Structural Characterization of Cu(I)/Zn(II)-metallothionein-3 by Ion Mobility Mass Spectrometry and Top-Down Mass Spectrometry.

ABSTRACT: Mammalian zinc metallothionein-3 (Zn₇MT3) plays an important role in protecting against copper toxicity by scavenging free Cu(II) ions or removing Cu(II) bound to β-amyloid and α-synuclein. While previous studies reported that Zn₇MT3 reacts with Cu(II) ions to form Cu(I)₄Zn(II)₄MT3ox containing two disulfides (ox), the precise localization of the metal ions and disulfides remained unclear. Here, we undertook comprehensive structural characterization of the metal-protein complexes formed by the reaction between Zn₇MT3 and Cu(II) ions using native ion mobility mass spectrometry (IM-MS). The complex formation mechanism was found to involve the disassembly of Zn₃S₉ and Zn₄S₁₁ clusters from Zn

SUBMITTER: Peris-Diaz MD 

PROVIDER: S-EPMC10372872 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature